ID   KEX1_PARBP              Reviewed;         635 AA.
AC   C0SGJ2;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 43.
DE   RecName: Full=Pheromone-processing carboxypeptidase KEX1;
DE            EC=3.4.16.6;
DE   AltName: Full=Carboxypeptidase D;
DE   Flags: Precursor;
GN   Name=KEX1; ORFNames=PABG_06619;
OS   Paracoccidioides brasiliensis (strain Pb03).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX   NCBI_TaxID=482561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pb03;
RX   PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA   Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA   Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA   Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA   Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA   Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA   Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA   Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA   Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT   "Comparative genomic analysis of human fungal pathogens causing
RT   paracoccidioidomycosis.";
RL   PLoS Genet. 7:E1002345-E1002345(2011).
CC   -!- FUNCTION: Protease with a carboxypeptidase B-like function involved in
CC       the C-terminal processing of the lysine and arginine residues from
CC       protein precursors. Promotes cell fusion and is involved in the
CC       programmed cell death (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential release of a C-terminal arginine or lysine
CC         residue.; EC=3.4.16.6;
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC       {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
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DR   EMBL; KN305543; EEH16532.1; -; Genomic_DNA.
DR   AlphaFoldDB; C0SGJ2; -.
DR   SMR; C0SGJ2; -.
DR   MEROPS; S10.007; -.
DR   EnsemblFungi; EEH16532; EEH16532; PABG_06619.
DR   VEuPathDB; FungiDB:PABG_06619; -.
DR   HOGENOM; CLU_008523_11_0_1; -.
DR   InParanoid; C0SGJ2; -.
DR   Proteomes; UP000002740; Unassembled WGS sequence.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001563; Peptidase_S10.
DR   PANTHER; PTHR11802; PTHR11802; 1.
DR   Pfam; PF00450; Peptidase_S10; 1.
DR   PRINTS; PR00724; CRBOXYPTASEC.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   3: Inferred from homology;
KW   Apoptosis; Carboxypeptidase; Glycoprotein; Golgi apparatus; Hydrolase;
KW   Membrane; Protease; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..635
FT                   /note="Pheromone-processing carboxypeptidase KEX1"
FT                   /id="PRO_0000411933"
FT   TOPO_DOM        28..514
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        515..535
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        536..635
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          472..500
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          579..635
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        179
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        381
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        443
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        112
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        432
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        440
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        492
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   635 AA;  71017 MW;  BFDDCC0A0233F0A6 CRC64;
     MGFSGSRAWS KWLTICLAIT HPFSVTAKSA ADYYVHSLPG QPEGPLLKMH AGHIEISPET
     SGNLFFWHFE NRHIADKPRT VVWLNGGPGC SSEDGALMEI GPYRLIDKET LNYTEGSWDE
     FANLLFVDQP VGTGFSYGST EHYVHELDEM ASQFVTFLEK WFEIFPHYEP DDLYFAGESY
     AGQYIPYIAR AVLDRNKKQD VQANNRIWNL KGLLIGNGWI SPQHQYPAYL PYVYQEGVVQ
     AGTQEANLIE AKAAKCMKEL NVEDTTGTVH IPDCEDILQA ILDYTHKGKR CINMYDIRLT
     DDYSACGMNW PPDLRDIQPY LRRKDVVKAL HINEEKQTGW TECAGAVGSS LKARNSKPAV
     ELLPGLLEEG LPILLFSGQK DLICNHVGTE DMIKNMKWSG GTGFELSPGV WAPRQDWTFE
     GEPAGIYQQA RNLTYVLFYN ASHMVPFDYP RRSRDMLDKF LGVDITHIGG DPADSRIDGE
     KGPTTSVGAH PNSTAAAERE KEKLNTAAWK AYYKSGEVAL VIVAIAAFAW GIFIWRSRRK
     HQSSGYRSIY PMLGLNSTGS LGQISHKHSR RNGDIEAADF DETELDDQPS QAFLSRSSRD
     GDAYAVGEES SDEEDGASDG QQPMFDQSRG EEGRS